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P35128

- UBE2N_DROME

UniProt

P35128 - UBE2N_DROME

Protein

Ubiquitin-conjugating enzyme E2 N

Gene

ben

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    Catalyzes the covalent attachment of ubiquitin to other proteins.

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei87 – 871Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: FlyBase
    4. ubiquitin protein ligase binding Source: FlyBase
    5. ubiquitin-protein transferase activity Source: FlyBase

    GO - Biological processi

    1. axonogenesis Source: FlyBase
    2. axon target recognition Source: FlyBase
    3. flight behavior Source: FlyBase
    4. grooming behavior Source: FlyBase
    5. jump response Source: FlyBase
    6. photoreceptor cell morphogenesis Source: FlyBase
    7. positive regulation of mitotic cell cycle, embryonic Source: FlyBase
    8. response to anesthetic Source: FlyBase
    9. synapse maturation Source: FlyBase
    10. synaptic growth at neuromuscular junction Source: FlyBase

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiP35128.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 N (EC:6.3.2.19)
    Alternative name(s):
    Protein bendless
    Ubiquitin carrier protein N
    Ubiquitin-conjugating enzyme E2-17 kDa
    Ubiquitin-protein ligase D3
    Ubiquitin-protein ligase N
    Gene namesi
    Name:ben
    Synonyms:UbcD3
    ORF Names:CG18319
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0000173. ben.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: FlyBase
    2. perinuclear region of cytoplasm Source: FlyBase
    3. UBC13-UEV1A complex Source: FlyBase

    Pathology & Biotechi

    Disruption phenotypei

    Mutants in this gene exhibit several, largely neuronal defects including lesions affecting the neuronal connectivity of the giant fiber with the "jumping muscle", and the axons of photoreceptor cells R7 and R8 fail to make the proper right-angle turn into the medulla (hence the term "bendless").1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151Ubiquitin-conjugating enzyme E2 NPRO_0000082521Add
    BLAST

    Proteomic databases

    PaxDbiP35128.
    PRIDEiP35128.

    Expressioni

    Gene expression databases

    BgeeiP35128.

    Interactioni

    Protein-protein interaction databases

    BioGridi58728. 4 interactions.
    DIPiDIP-22866N.
    MINTiMINT-1003000.
    STRINGi7227.FBpp0289793.

    Structurei

    3D structure databases

    ProteinModelPortaliP35128.
    SMRiP35128. Positions 4-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00540000070023.
    InParanoidiP35128.
    KOiK10580.
    OMAiDVAKHYK.
    OrthoDBiEOG7XWPQB.
    PhylomeDBiP35128.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P35128-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSLPRRIIK ETQRLMQEPV PGINAIPDEN NARYFHVIVT GPNDSPFEGG    50
    VFKLELFLPE DYPMSAPKVR FITKIYHPNI DRLGRICLDV LKDKWSPALQ 100
    IRTILLSIQA LLSAPNPDDP LANDVAELWK VNEAEAIRNA REWTQKYAVE 150
    D 151
    Length:151
    Mass (Da):17,236
    Last modified:February 1, 1994 - v1
    Checksum:i1D096E72A7AEA420
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20126 mRNA. Translation: AAA28392.1.
    S70118 mRNA. Translation: AAB30753.1.
    EU217226 Genomic DNA. Translation: ABW92183.1.
    EU217227 Genomic DNA. Translation: ABW92184.1.
    EU217228 Genomic DNA. Translation: ABW92185.1.
    EU217229 Genomic DNA. Translation: ABW92186.1.
    EU217230 Genomic DNA. Translation: ABW92187.1.
    EU217231 Genomic DNA. Translation: ABW92188.1.
    EU217232 Genomic DNA. Translation: ABW92189.1.
    EU217233 Genomic DNA. Translation: ABW92190.1.
    EU217234 Genomic DNA. Translation: ABW92191.1.
    EU217235 Genomic DNA. Translation: ABW92192.1.
    EU217236 Genomic DNA. Translation: ABW92193.1.
    EU217237 Genomic DNA. Translation: ABW92194.1.
    AE014298 Genomic DNA. Translation: AAF48338.1.
    AY069527 mRNA. Translation: AAL39672.1.
    PIRiS35793.
    RefSeqiNP_001162752.1. NM_001169281.1.
    NP_001245663.1. NM_001258734.1.
    NP_001259540.1. NM_001272611.1.
    NP_001259541.1. NM_001272612.1.
    NP_511150.1. NM_078595.2.
    UniGeneiDm.2088.

    Genome annotation databases

    EnsemblMetazoaiFBtr0073855; FBpp0073686; FBgn0000173.
    FBtr0300566; FBpp0289793; FBgn0000173.
    FBtr0307296; FBpp0298297; FBgn0000173.
    FBtr0332843; FBpp0305066; FBgn0000173.
    FBtr0332844; FBpp0305067; FBgn0000173.
    GeneIDi32358.
    KEGGidme:Dmel_CG18319.
    UCSCiCG18319-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20126 mRNA. Translation: AAA28392.1 .
    S70118 mRNA. Translation: AAB30753.1 .
    EU217226 Genomic DNA. Translation: ABW92183.1 .
    EU217227 Genomic DNA. Translation: ABW92184.1 .
    EU217228 Genomic DNA. Translation: ABW92185.1 .
    EU217229 Genomic DNA. Translation: ABW92186.1 .
    EU217230 Genomic DNA. Translation: ABW92187.1 .
    EU217231 Genomic DNA. Translation: ABW92188.1 .
    EU217232 Genomic DNA. Translation: ABW92189.1 .
    EU217233 Genomic DNA. Translation: ABW92190.1 .
    EU217234 Genomic DNA. Translation: ABW92191.1 .
    EU217235 Genomic DNA. Translation: ABW92192.1 .
    EU217236 Genomic DNA. Translation: ABW92193.1 .
    EU217237 Genomic DNA. Translation: ABW92194.1 .
    AE014298 Genomic DNA. Translation: AAF48338.1 .
    AY069527 mRNA. Translation: AAL39672.1 .
    PIRi S35793.
    RefSeqi NP_001162752.1. NM_001169281.1.
    NP_001245663.1. NM_001258734.1.
    NP_001259540.1. NM_001272611.1.
    NP_001259541.1. NM_001272612.1.
    NP_511150.1. NM_078595.2.
    UniGenei Dm.2088.

    3D structure databases

    ProteinModelPortali P35128.
    SMRi P35128. Positions 4-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58728. 4 interactions.
    DIPi DIP-22866N.
    MINTi MINT-1003000.
    STRINGi 7227.FBpp0289793.

    Proteomic databases

    PaxDbi P35128.
    PRIDEi P35128.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0073855 ; FBpp0073686 ; FBgn0000173 .
    FBtr0300566 ; FBpp0289793 ; FBgn0000173 .
    FBtr0307296 ; FBpp0298297 ; FBgn0000173 .
    FBtr0332843 ; FBpp0305066 ; FBgn0000173 .
    FBtr0332844 ; FBpp0305067 ; FBgn0000173 .
    GeneIDi 32358.
    KEGGi dme:Dmel_CG18319.
    UCSCi CG18319-RA. d. melanogaster.

    Organism-specific databases

    CTDi 32358.
    FlyBasei FBgn0000173. ben.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00540000070023.
    InParanoidi P35128.
    KOi K10580.
    OMAi DVAKHYK.
    OrthoDBi EOG7XWPQB.
    PhylomeDBi P35128.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    SignaLinki P35128.

    Miscellaneous databases

    ChiTaRSi GTF2IRD1. drosophila.
    GenomeRNAii 32358.
    NextBioi 778098.

    Gene expression databases

    Bgeei P35128.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes."
      Muralidhar M., Thomas J.B.
      Neuron 11:253-266(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE.
    2. "Bendless, a Drosophila gene affecting neuronal connectivity, encodes a ubiquitin-conjugating enzyme homolog."
      Oh C.E., McMahon R., Benzer S., Tanouye M.A.
      J. Neurosci. 14:3166-3179(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Hitchhiking effects of recurrent beneficial amino acid substitutions in the Drosophila melanogaster genome."
      Andolfatto P.
      Genome Res. 17:1755-1762(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ZW104, ZW109, ZW122, ZW123, ZW133, ZW136, ZW139, ZW140, ZW141, ZW142, ZW143 and ZW144.
    4. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.

    Entry informationi

    Entry nameiUBE2N_DROME
    AccessioniPrimary (citable) accession number: P35128
    Secondary accession number(s): A9YHJ7, Q9VY67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3